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J Biol Chem. 2018 May 4;293(18):6751-6761. doi: 10.1074/jbc.M117.819391. Epub 2018 Mar 16.

14-3-3 proteins tune non-muscle myosin II assembly.

Author information

From the Departments of Cell Biology.
From the Departments of Cell Biology,
Pharmacology and Molecular Sciences, and.
Medicine, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205.


The 14-3-3 family comprises a group of small proteins that are essential, ubiquitous, and highly conserved across eukaryotes. Overexpression of the 14-3-3 proteins σ, ϵ, ζ, and η correlates with high metastatic potential in multiple cancer types. In Dictyostelium, 14-3-3 promotes myosin II turnover in the cell cortex and modulates cortical tension, cell shape, and cytokinesis. In light of the important roles of 14-3-3 proteins across a broad range of eukaryotic species, we sought to determine how 14-3-3 proteins interact with myosin II. Here, conducting in vitro and in vivo studies of both Dictyostelium (one 14-3-3 and one myosin II) and human proteins (seven 14-3-3s and three nonmuscle myosin IIs), we investigated the mechanism by which 14-3-3 proteins regulate myosin II assembly. Using in vitro assembly assays with purified myosin II tail fragments and 14-3-3, we demonstrate that this interaction is direct and phosphorylation-independent. All seven human 14-3-3 proteins also altered assembly of at least one paralog of myosin II. Our findings indicate a mechanism of myosin II assembly regulation that is mechanistically conserved across a billion years of evolution from amebas to humans. We predict that altered 14-3-3 expression in humans inhibits the tumor suppressor myosin II, contributing to the changes in cell mechanics observed in many metastatic cancers.


14-3-3 protein; Dictyostelium; bipolar filament assembly; cytoskeleton; fluorescence correlation spectroscopy (FCS); human; myosin; surface plasmon resonance (SPR)

[Available on 2019-05-04]
[Indexed for MEDLINE]

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